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BCKDK BCKDK BCKDHB BCKDHB LIPT1 LIPT1 BCKDHA BCKDHA PDHA1 PDHA1 PGLYRP3 PGLYRP3 DBT DBT ALDH1A1 ALDH1A1 DLAT DLAT ACO2 ACO2 GCSH GCSH PDHB PDHB DLD DLD OGDH OGDH DLST DLST PDHX PDHX ACLY ACLY ALDH3A1 ALDH3A1 DHTKD1 DHTKD1 OGDHL OGDHL ACO1 ACO1 ALDH3A2 ALDH3A2 IREB2 IREB2 MRPS36 MRPS36 ALDH5A1 ALDH5A1 AADAT AADAT
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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small nodes:
protein of unknown 3D structure
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large nodes:
some 3D structure is known or predicted
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query proteins and first shell of interactors
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white nodes:
second shell of interactors
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experimentally determined
Predicted Interactions
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textmining
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DLDdihydrolipoamide dehydrogenase; Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (509 aa)
ACO2aconitase 2, mitochondrial; Catalyzes the isomerization of citrate to isocitrate via cis-aconitate (By similarity) (780 aa)
BCKDKbranched chain ketoacid dehydrogenase kinase; Catalyzes the phosphorylation and inactivation of the branched-chain alpha-ketoacid dehydrogenase complex, the key regulatory enzyme of the valine, leucine and isoleucine catabolic pathways. Key enzyme that regulate the activity state of the BCKD complex (By similarity) (412 aa)
OGDHoxoglutarate (alpha-ketoglutarate) dehydrogenase (lipoamide); The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components- 2- oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (1023 aa)
ALDH3A1aldehyde dehydrogenase 3 family, member A1; ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. This protein preferentially oxidizes aromatic aldehyde substrates. It may play a role in the oxidation of toxic aldehydes (453 aa)
AADATaminoadipate aminotransferase; Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino- group acceptors, with a preference for 2-oxoglutarate, 2- oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro) (425 aa)
PDHXpyruvate dehydrogenase complex, component X; Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex (501 aa)
ACLYATP citrate lyase; ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine (1101 aa)
MRPS36mitochondrial ribosomal protein S36 (103 aa)
IREB2iron-responsive element binding protein 2; RNA-binding protein that binds to iron-responsive elements (IRES), which are stem-loop structures found in the 5’- UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3’-UTR of transferrin receptor mRNA. Binding to the IRE element in ferritin results in the repression of its mRNA translation. Binding of the protein to the transferrin receptor mRNA inhibits the degradation of this otherwise rapidly degraded mRNA (963 aa)
DHTKD1dehydrogenase E1 and transketolase domain containing 1; The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components- 2- oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity) (919 aa)
BCKDHAbranched chain keto acid dehydrogenase E1, alpha polypeptide; The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components- branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (445 aa)
DLATdihydrolipoamide S-acetyltransferase; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle (647 aa)
PGLYRP3peptidoglycan recognition protein 3; Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Binds also to Gram- negative bacteria, and has bacteriostatic activity towards Gram- negative bacteria. Plays a role in innate immunity (341 aa)
ALDH1A1aldehyde dehydrogenase 1 family, member A1; Binds free retinal and cellular retinol-binding protein- bound retinal. Can convert/oxidize retinaldehyde to retinoic acid (By similarity) (501 aa)
PDHBpyruvate dehydrogenase (lipoamide) beta; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle (359 aa)
ACO1aconitase 1, soluble; Iron sensor. Binds a 4Fe-4S cluster and functions as aconitase when cellular iron levels are high. Functions as mRNA binding protein that regulates uptake, sequestration and utilization of iron when cellular iron levels are low. Binds to iron-responsive elements (IRES) in target mRNA species when iron levels are low. Binding of a 4Fe-4S cluster precludes RNA binding (889 aa)
ALDH5A1aldehyde dehydrogenase 5 family, member A1; Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA) (548 aa)
BCKDHBbranched chain keto acid dehydrogenase E1, beta polypeptide; The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components- branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (392 aa)
GCSHglycine cleavage system protein H (aminomethyl carrier); The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein (173 aa)
DLSTdihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex); The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components- 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (453 aa)
LIPT1lipoyltransferase 1; Catalyzes the transfer of the lipoyl group from lipoyl- AMP to the specific lysine residue of lipoyl domains of lipoate- dependent enzymes (By similarity) (373 aa)
ALDH3A2aldehyde dehydrogenase 3 family, member A2; Catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Active on a variety of saturated and unsaturated aliphatic aldehydes between 6 and 24 carbons in length. Responsible for conversion of the sphingosine 1-phosphate (S1P) degradation product hexadecenal to hexadecenoic acid (508 aa)
DBTdihydrolipoamide branched chain transacylase E2; The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components- branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (482 aa)
OGDHLoxoglutarate dehydrogenase-like (1010 aa)
PDHA1pyruvate dehydrogenase (lipoamide) alpha 1 (428 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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